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Purification and crystallization of the catalytic PRONE domain of RopGEF8 and its complex with Rop4 from Arabidopsis thaliana

The PRONE domain of the guanine nucleotide exchange factor RopGEF8 (PRONE8) was purified and crystallized free and in complex with the Rho-family protein Rop4 using the hanging-drop vapour-diffusion method. PRONE8 crystals were obtained using NaCl as precipitating agent and belong to the hexagonal s...

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Detaylı Bibliyografya
Asıl Yazarlar: Thomas, Christoph, Weyand, Michael, Wittinghofer, Alfred, Berken, Antje
Materyal Türü: Artigo
Dil:Inglês
Baskı/Yayın Bilgisi: International Union of Crystallography 2006
Konular:
Online Erişim:https://ncbi.nlm.nih.gov/pmc/articles/PMC2243088/
https://ncbi.nlm.nih.gov/pubmed/16754995
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1107/S1744309106018689
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